Autodisplay Biotech GmbH

Dusseldorf, Germany

Autodisplay Biotech GmbH

Dusseldorf, Germany
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Festel G.,Festel Capital | Festel G.,Butalco GmbH | Festel G.,ETH Zurich | Festel G.,Autodisplay Biotech GmbH | And 5 more authors.
Journal of Cleaner Production | Year: 2014

Competitive production costs compared to conventional fuels are imperative for biofuels to gain market shares, as current tax advantages for biofuels are only temporary. Comparing production costs of different biofuels with fossil fuels is a challenge due to the complexity of influencing factors. The objective of this research paper is threefold: 1) to project future bio-fuel feedstock prices based on the crude oil price development, the price index for agricultural products, growth in world population, growth in wealth per capita income, and change in energy consumption per capita, 2) to simulate production costs under consideration of likely economies of scale from scaling-up production size and technological learning and 3) to compare different biofuels and fossil fuels by scenario analysis. A calculation model for biofuel production is used to analyse projected production costs for different types of biofuels in Europe for 2015 and 2020. Unlike engineering oriented bottom-up approaches that are often used in other biofuel studies, the macro-economic top-down approach applied in this study enables an economic comparison and discussion of various fuel types based on reference scenarios of crude oil prices of €50, €100, €150 and €200 per barrel. Depending on the specific raw material prices as well as the conversion costs, the analysis delivered a differentiated view on the production costs and thus on the competitiveness of each individual type of fuel. The results show that 2nd generation biofuels are most likely to achieve competitive production costs mid- to long-term when taking into account the effects from technological learning and production scale size as well as crude oil price scenarios between €50 and €200 per barrel for both reference years. In all crude oil price scenarios, bioethanol from lignocellulosic raw materials as well as biodiesel from waste oil are associated with high cost saving potentials which enable them to outperform fossil fuels and 1st generation biofuels. © 2013 Elsevier Ltd. All rights reserved.

Festel G.,Autodisplay Biotech GmbH | Maas R.,Autodisplay Biotech GmbH
Journal of Commercial Biotechnology | Year: 2012

An increasing number of chemicals and materials like base chemicals and polymers as well as high value products such as consumer chemicals and specialty chemicals are produced using biotechnology in one or more of the process steps. In 2010 the sale volume of biotechnology products was around 92 billion Euro worldwide. Sales are estimated to increase to around 228 billion Euro in 2015 and to around 515 billion Euro in 2020. On a sector level the largest market potential lies in the production of biopolymers and active pharmaceutical ingredients. Aas a rule commercial development is mainly driven by multinational enterprises whereas small and medium enterprises contribute primarily to the technological development. Especially the latter group faces several challenges during their development. These mainly concern business models and growth strategies as well as financing strategies and resources. Investors have not yet fully identified the area of industrial biotechnology as an attractive investment field but they could become a major capital source as they start to understand more the potential of industrial biotechnology.

Detzel C.,University of Munster | Detzel C.,Autodisplay Biotech GmbH | Maas R.,University of Munster | Maas R.,Autodisplay Biotech GmbH | And 2 more authors.
Applied Microbiology and Biotechnology | Year: 2013

Using the Autodisplay system, a recombinant Escherichia coli strain displaying the dimeric nitrilase from Klebsiella pneumoniae subsp. ozaenae (NitKp) on the cell surface was constructed. Localization of the nitrilase in the cell envelope of E. coli was monitored by sodium dodecyl sulfate polyacrylamide gel electrophoresis and surface exposure was verified by its accessibility to externally added protease. The whole-cell biocatalyst obtained converted the substrates analyzed in the following order: chloroxynil > bromoxynil > ioxynil > 3-bromo-4-hydroxybenzonitrile (1.67, 0.89, 0.13, and 0.09 mM product formation within 72 h, respectively), indicating the same substrate specificity for the displayed enzyme as for the free enzyme. The whole-cell biocatalyst was also able to convert 3-fluoro-4-hydroxybenzonitrile and 3,5-dimethyl-4-hydroxybenzonitrile to the corresponding carboxylic acids. In contrast, it was not possible to detect any enzyme activity when 4-methoxybenzonitrile was used as substrate. The temperature optimum determined was 45 °C for the surface-displayed enzyme instead of 35 °C for the purified enzyme. In addition, the optimum activity of the displayed nitrilase was shifted to more acidic pH in comparison to the free enzyme. © 2012 Springer-Verlag.

Jose J.,University of Munster | Maas R.M.,Autodisplay Biotech GmbH | Teese M.G.,University of Munster
Journal of Biotechnology | Year: 2012

To display an enzyme on the surface of a living cell is an important step forward towards a broader use of biocatalysts. Enzymes immobilized on surfaces appeared to be more stable compared to free molecules. It is possible by standard techniques to let the bacterial cell (e.g. Escherichia coli) decorate its surface with the enzyme and produce it on high amounts with a minimum of costs and equipment. Moreover, these cells can be recovered and reused in several subsequent process cycles. Among other systems, autodisplay has some extra features that could overcome limitations in the industrial applications of enzymes. One major advantage of autodisplay is the motility of the anchoring domain. Enzyme subunits exposed at the cell surface having affinity to each other will spontaneously form dimers or multimers. Using autodisplay enzymes with prosthetic groups can be displayed, expanding the application of surface display to the industrial important P450 enzymes. Finally, up to 105-106 enzyme molecules can be displayed on a single cell. In the present review, we summarize recent achievements in the autodisplay of enzymes with particular attention to industrial needs and process development. Applications that will provide sustainable solutions towards a bio-based industry are discussed. © 2012 Elsevier B.V.

Detzel C.,Heinrich Heine University Düsseldorf | Maas R.,Heinrich Heine University Düsseldorf | Maas R.,Autodisplay Biotech GmbH | Jose J.,Heinrich Heine University Düsseldorf
ChemCatChem | Year: 2011

In the present study, a whole cell biocatalyst for the synthesis of (R)-mandelic acid from mandelonitrile was constructed. For this purpose, nitrilase from Alcaligenes faecalis subsp. faecalis ATCC 8750 was displayed on the surface of Escherichia coli by using Autodisplay. Localization of the nitrilase in the cell envelope of E. coli was monitored by SDS-PAGE and surface exposure was verified by its accessibility to externally added protease. The whole cell biocatalyst converted up to 2.6mM of (R)-mandelic acid under optimum conditions at pH7.5 and 45°C within 24h (1mL culture, OD 578=10). By using chiral HPLC, the ee value of the product was determined to be >99%. The surface displayed nitrilase showed an apparent K m value of 3.6mM and an apparent V max value of 1nmolmin -1mL -1 when a bacterial suspension of OD 578 3 was used. Substrate inhibition by benzaldehyde was similar to that of the free enzyme. The whole-cell biocatalyst retained 55% of its initial (R)-mandelic acid production after 5 cycles of repeated use, and could be stored at -70°C for 180d without a substantial loss of activity. In addition the whole cell biocatalyst converted 9.3mM phenylacetonitrile within 16h. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Kranen E.,Heinrich Heine University Düsseldorf | Steffan N.,University of Marburg | Maas R.,Autodisplay Biotech GmbH | Li S.-M.,University of Marburg | Jose J.,Heinrich Heine University Düsseldorf
ChemCatChem | Year: 2011

The following study depicts the development of a whole cell biocatalyst for the prenylation of indole derivatives. For this purpose the prenyltransferase FgaPT2 from Aspergillus fumigatus was displayed on the surface of Escherichia coli cells by using Autodisplay. The presence of the prenyltransferase in the outer membrane was detected by using SDS-PAGE and Western Blot after the proteins of the outer membrane were isolated. The orientation of the prenyltransferase towards the outside of the cells was investigated by accessibility testing with externally added proteases. The FgaPT2 whole cell biocatalyst converted up to 250μM of indole-3-propionic acid, approximately 25% of the substrate used in the assay (100μL sample, OD 578=40). Another indole substrate, L-β-homotryptophan was also investigated and a conversion of 13% was determined. By optimizing the assay conditions the conversion rate could be raised to approximately 30% of indole-3-propionic acid during a 24h incubation time at 20°C. The whole cell biocatalyst endured a storage period of one month at 8°C without any detectable loss in activity. Reusability was confirmed by recycling the biocatalyst. After three cycles of consecutive use, the whole cell biocatalyst retained a conversion rate of 46% of indole-3-propionic acid and 23% of L-β-homotryptophan after the third cycle. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Kranen E.,Autodisplay Biotech GmbH | Detzel C.,Autodisplay Biotech GmbH | Weber T.,Henkel AG | Jose J.,University of Munster
Microbial Cell Factories | Year: 2014

Background: Lipases including the lipase from Burkholderia cepacia are in a main focus in biotechnology research since many years because of their manifold possibilities for application in industrial processes. The application of Burkholderia cepacia lipase for these processes appears complicated because of the need for support by a chaperone, the lipase specific foldase. Purification and reconstitution protocols therefore interfere with an economic implementation of such enzymes in industry. Autodisplay is a convenient method to express a variety of passenger proteins on the surface of E. coli. This method makes subsequent purification steps to obtain the protein of interest unnecessary. If enzymes are used as passengers, the corresponding cells can simply be applied as whole cell biocatalysts. Furthermore, enzymes surface displayed in this manner often acquire stabilization by anchoring within the outer membrane of E. coli.Results: The lipase and its chaperone foldase from B. cepacia were co-expressed on the surface of E. coli via autodisplay. The whole cell biocatalyst obtained thereby exhibited an enzymatic activity of 2.73 mU mL-1 towards the substrate p-nitrophenyl palmitate when applied in an OD578 =1. Outer membrane fractions prepared from the same culture volume showed a lipase activity of 4.01 mU mL-1. The lipase-whole cell biocatalyst as well as outer membrane preparations thereof were used in a standardized laundry test, usually adopted to determine the power of washing agents. In this test, the lipase whole cell biocatalyst and the membrane preparation derived thereof exhibited the same lipolytic activity as the purified lipase from B. cepacia and a lipase preparation which is already applied in commercial washing agents.Conclusions: Co-expression of both the lipase and its chaperone foldase on the surface of E. coli yields a lipid degrading whole cell biocatalyst. Therefore the chaperone supported folding process, absolutely required for the lipolytic activity appears not to be hindered by surface display. Furthermore, the cells and the membrane preparations appeared to be stable enough to endure a European standard laundry test and show efficient fat removal properties herein. © 2014 Kranen et al.; licensee BioMed Central Ltd.

Autodisplay Biotech GmbH | Date: 2010-09-09

The present invention refers to a method for binding a recombinant polypeptide to a carrier, wherein a layer is bound to a carrier, and the layer comprises a recombinant polypeptide on the surface distal to the carrier.

The present invention relates to a method for the surface display of a recombinant polypeptide on the surface of a host cell, said method comprising the steps: (a) providing a host cell transformed with a nucleic acid fusion operatively linked with an expression control sequence, said nucleic acid fusion comprising: (i) a portion encoding a signal peptide, (ii) a portion encoding the recombinant polypeptide to be displayed, (iii) a portion encoding a transmembrane linker, and (iv) a portion encoding the trans porter domain of an EhaA protein, and (b) culturing the host cell under conditions wherein the nucleic acid fusion is expressed and the expression product comprising the recombinant polypeptide is displayed on the surface of the host cell.

Autodisplay Biotech GmbH | Date: 2011-09-22

The present invention relates to a method for the display of recombinant functional polypeptides containing a prosthetic group selected from metal porphyrin and flavin containing groups on the surface of a host cell using the transporter domain of an autotransporter.

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